dbPTM

HNRH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HNRH1_HUMAN
UniProt AC	P31943
Protein Name	Heterogeneous nuclear ribonucleoprotein H
Gene Name	HNRNPH1
Organism	Homo sapiens (Human).
Sequence Length	449
Subcellular Localization	Nucleus, nucleoplasm.
Protein Description	This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG)..
Protein Sequence	MMLGTEGGEGFVVKVRGLPWSCSADEVQRFFSDCKIQNGAQGIRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNNVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYNGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSTFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEDAVAAMSKDKANMQHRYVELFLNSTAGASGGAYEHRYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDFQSNIA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MMLGTEGG -------CCCCCCCC	4.52	22814378
1	Sulfoxidation	-------MMLGTEGG -------CCCCCCCC	4.52	28465586
2	Acetylation	------MMLGTEGGE ------CCCCCCCCC	4.80	22223895
2	Sulfoxidation	------MMLGTEGGE ------CCCCCCCCC	4.80	28465586
5	Phosphorylation	---MMLGTEGGEGFV ---CCCCCCCCCEEE	27.74	20860994
14	Sumoylation	GGEGFVVKVRGLPWS CCCEEEEEEECCCCC	22.40	-
14	Sumoylation	GGEGFVVKVRGLPWS CCCEEEEEEECCCCC	22.40	-
14	Ubiquitination	GGEGFVVKVRGLPWS CCCEEEEEEECCCCC	22.40	-
21	Phosphorylation	KVRGLPWSCSADEVQ EEECCCCCCCHHHHH	9.03	25159151
22	Glutathionylation	VRGLPWSCSADEVQR EECCCCCCCHHHHHH	3.25	22555962
22	S-palmitoylation	VRGLPWSCSADEVQR EECCCCCCCHHHHHH	3.25	26865113
23	Phosphorylation	RGLPWSCSADEVQRF ECCCCCCCHHHHHHH	32.99	25159151
29	Methylation	CSADEVQRFFSDCKI CCHHHHHHHHHCCEE	39.49	115479139
34	S-nitrosocysteine	VQRFFSDCKIQNGAQ HHHHHHCCEECCCCC	3.97	-
34	S-nitrosylation	VQRFFSDCKIQNGAQ HHHHHHCCEECCCCC	3.97	19483679
35	Sumoylation	QRFFSDCKIQNGAQG HHHHHCCEECCCCCE	52.93	-
35	Acetylation	QRFFSDCKIQNGAQG HHHHHCCEECCCCCE	52.93	25953088
35	Sumoylation	QRFFSDCKIQNGAQG HHHHHCCEECCCCCE	52.93	28112733
35	Ubiquitination	QRFFSDCKIQNGAQG HHHHHCCEECCCCCE	52.93	21906983
44	Methylation	QNGAQGIRFIYTREG CCCCCEEEEEEEECC	20.80	54556625
47	Phosphorylation	AQGIRFIYTREGRPS CCEEEEEEEECCCCC	9.31	24719451
54	Phosphorylation	YTREGRPSGEAFVEL EEECCCCCCCEEEEE	48.15	22617229
63	Phosphorylation	EAFVELESEDEVKLA CEEEEECCHHHHEEE	64.07	19664994
68	Sumoylation	LESEDEVKLALKKDR ECCHHHHEEEEHHCH	26.45	-
72	Sumoylation	DEVKLALKKDRETMG HHHEEEEHHCHHHHC	47.20	-
72	Sumoylation	DEVKLALKKDRETMG HHHEEEEHHCHHHHC	47.20	-
81	Methylation	DRETMGHRYVEVFKS CHHHHCCEEEEEHHC	31.31	-
87	Sumoylation	HRYVEVFKSNNVEMD CEEEEEHHCCCEEEE	58.40	28112733
87	Ubiquitination	HRYVEVFKSNNVEMD CEEEEEHHCCCEEEE	58.40	21890473
88	Phosphorylation	RYVEVFKSNNVEMDW EEEEEHHCCCEEEEE	23.36	21712546
98	2-Hydroxyisobutyrylation	VEMDWVLKHTGPNSP EEEEEEEEECCCCCC	29.51	-
98	Acetylation	VEMDWVLKHTGPNSP EEEEEEEEECCCCCC	29.51	21466224
98	Methylation	VEMDWVLKHTGPNSP EEEEEEEEECCCCCC	29.51	23644510
98	Sumoylation	VEMDWVLKHTGPNSP EEEEEEEEECCCCCC	29.51	28112733
98	Ubiquitination	VEMDWVLKHTGPNSP EEEEEEEEECCCCCC	29.51	21890473
100	Phosphorylation	MDWVLKHTGPNSPDT EEEEEEECCCCCCCC	53.39	23927012
104	Phosphorylation	LKHTGPNSPDTANDG EEECCCCCCCCCCCC	27.56	23927012
107	Phosphorylation	TGPNSPDTANDGFVR CCCCCCCCCCCCCEE	30.64	22167270
114	Methylation	TANDGFVRLRGLPFG CCCCCCEEECCCCCC	19.19	-
122	S-nitrosocysteine	LRGLPFGCSKEEIVQ ECCCCCCCCHHHHHH	5.56	-
122	S-nitrosylation	LRGLPFGCSKEEIVQ ECCCCCCCCHHHHHH	5.56	19483679
123	Phosphorylation	RGLPFGCSKEEIVQF CCCCCCCCHHHHHHH	43.40	22777824
151	Phosphorylation	PVDFQGRSTGEAFVQ CCCCCCCCHHHHHHH	47.81	18669648
152	O-linked_Glycosylation	VDFQGRSTGEAFVQF CCCCCCCHHHHHHHH	37.37	23301498
152	Phosphorylation	VDFQGRSTGEAFVQF CCCCCCCHHHHHHHH	37.37	30087585
161	Phosphorylation	EAFVQFASQEIAEKA HHHHHHHHHHHHHHH	29.63	28450419
167	Acetylation	ASQEIAEKALKKHKE HHHHHHHHHHHHHHH	50.42	23954790
167	Ubiquitination	ASQEIAEKALKKHKE HHHHHHHHHHHHHHH	50.42	21890473
170	Ubiquitination	EIAEKALKKHKERIG HHHHHHHHHHHHHHC	58.66	-
171	Ubiquitination	IAEKALKKHKERIGH HHHHHHHHHHHHHCH	61.84	-
180	Phosphorylation	KERIGHRYIEIFKSS HHHHCHHHHHHHHHC	9.38	20068231
185	Sumoylation	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	-
185	2-Hydroxyisobutyrylation	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	-
185	Acetylation	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	25825284
185	Methylation	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	21689879
185	Succinylation	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	23954790
185	Sumoylation	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	-
185	Ubiquitination	HRYIEIFKSSRAEVR HHHHHHHHHCCCCHH	53.86	21890473
186	Phosphorylation	RYIEIFKSSRAEVRT HHHHHHHHCCCCHHH	17.82	20068231
187	Phosphorylation	YIEIFKSSRAEVRTH HHHHHHHCCCCHHHC	35.78	20068231
193	Phosphorylation	SSRAEVRTHYDPPRK HCCCCHHHCCCCCHH	29.93	28796482
195	Phosphorylation	RAEVRTHYDPPRKLM CCCHHHCCCCCHHHH	29.54	28796482
199	Methylation	RTHYDPPRKLMAMQR HHCCCCCHHHHHCCC	50.56	-
200	Ubiquitination	THYDPPRKLMAMQRP HCCCCCHHHHHCCCC	48.68	21890473
206	Methylation	RKLMAMQRPGPYDRP HHHHHCCCCCCCCCC	25.67	-
210	Phosphorylation	AMQRPGPYDRPGAGR HCCCCCCCCCCCCCC	30.42	22461510
212	Dimethylation	QRPGPYDRPGAGRGY CCCCCCCCCCCCCCC	26.21	-
212	Methylation	QRPGPYDRPGAGRGY CCCCCCCCCCCCCCC	26.21	18961567
217	Dimethylation	YDRPGAGRGYNSIGR CCCCCCCCCCCCCCC	43.84	-
217	Methylation	YDRPGAGRGYNSIGR CCCCCCCCCCCCCCC	43.84	24396111
219	Phosphorylation	RPGAGRGYNSIGRGA CCCCCCCCCCCCCCC	12.36	-
221	Phosphorylation	GAGRGYNSIGRGAGF CCCCCCCCCCCCCCH	20.24	30576142
224	Dimethylation	RGYNSIGRGAGFERM CCCCCCCCCCCHHHH	30.07	-
224	Methylation	RGYNSIGRGAGFERM CCCCCCCCCCCHHHH	30.07	24383111
230	Dimethylation	GRGAGFERMRRGAYG CCCCCHHHHHCCCCC	22.96	-
230	Methylation	GRGAGFERMRRGAYG CCCCCHHHHHCCCCC	22.96	18960657
232	Methylation	GAGFERMRRGAYGGG CCCHHHHHCCCCCCC	39.85	26494631
233	Dimethylation	AGFERMRRGAYGGGY CCHHHHHCCCCCCCC	25.42	-
233	Methylation	AGFERMRRGAYGGGY CCHHHHHCCCCCCCC	25.42	12018757
236	Phosphorylation	ERMRRGAYGGGYGGY HHHHCCCCCCCCCCC	21.08	20090780
240	Phosphorylation	RGAYGGGYGGYDDYN CCCCCCCCCCCCCCC	15.62	20090780
243	Phosphorylation	YGGGYGGYDDYNGYN CCCCCCCCCCCCCCC	10.98	20090780
246	Phosphorylation	GYGGYDDYNGYNDGY CCCCCCCCCCCCCCC	13.95	17360941
249	Phosphorylation	GYDDYNGYNDGYGFG CCCCCCCCCCCCCCC	13.37	17360941
253	Phosphorylation	YNGYNDGYGFGSDRF CCCCCCCCCCCCCCC	16.49	20090780
257	Phosphorylation	NDGYGFGSDRFGRDL CCCCCCCCCCCCCCC	24.29	25348954
259	Dimethylation	GYGFGSDRFGRDLNY CCCCCCCCCCCCCCC	37.30	-
259	Methylation	GYGFGSDRFGRDLNY CCCCCCCCCCCCCCC	37.30	30759959
262	Dimethylation	FGSDRFGRDLNYCFS CCCCCCCCCCCCCCC	42.40	-
262	Methylation	FGSDRFGRDLNYCFS CCCCCCCCCCCCCCC	42.40	30759953
266	Phosphorylation	RFGRDLNYCFSGMSD CCCCCCCCCCCCCCC	11.36	21945579
267	S-nitrosocysteine	FGRDLNYCFSGMSDH CCCCCCCCCCCCCCC	1.81	-
267	Glutathionylation	FGRDLNYCFSGMSDH CCCCCCCCCCCCCCC	1.81	22555962
267	S-nitrosylation	FGRDLNYCFSGMSDH CCCCCCCCCCCCCCC	1.81	22178444
269	Phosphorylation	RDLNYCFSGMSDHRY CCCCCCCCCCCCCCC	29.99	21945579
272	Phosphorylation	NYCFSGMSDHRYGDG CCCCCCCCCCCCCCC	33.52	23401153
276	Phosphorylation	SGMSDHRYGDGGSTF CCCCCCCCCCCCCCC	19.02	28152594
281	Phosphorylation	HRYGDGGSTFQSTTG CCCCCCCCCCCCCCC	31.42	23401153
282	Phosphorylation	RYGDGGSTFQSTTGH CCCCCCCCCCCCCCC	29.03	29978859
285	Phosphorylation	DGGSTFQSTTGHCVH CCCCCCCCCCCCCEE	24.60	26330541
286	Phosphorylation	GGSTFQSTTGHCVHM CCCCCCCCCCCCEEE	26.47	28555341
287	Phosphorylation	GSTFQSTTGHCVHMR CCCCCCCCCCCEEEC	30.12	26330541
290	Glutathionylation	FQSTTGHCVHMRGLP CCCCCCCCEEECCCC	2.08	22555962
294	Methylation	TGHCVHMRGLPYRAT CCCCEEECCCCCCCC	28.72	115385249
298	Phosphorylation	VHMRGLPYRATENDI EEECCCCCCCCCCCC	20.23	20090780
301	O-linked_Glycosylation	RGLPYRATENDIYNF CCCCCCCCCCCCHHC	26.73	23301498
301	Phosphorylation	RGLPYRATENDIYNF CCCCCCCCCCCCHHC	26.73	27987026
306	Phosphorylation	RATENDIYNFFSPLN CCCCCCCHHCCCCCC	14.58	29255136
310	O-linked_Glycosylation	NDIYNFFSPLNPVRV CCCHHCCCCCCCEEE	25.08	23301498
310	Phosphorylation	NDIYNFFSPLNPVRV CCCHHCCCCCCCEEE	25.08	29255136
328	Phosphorylation	IGPDGRVTGEADVEF ECCCCCCCEECEEEE	28.13	-
346	Phosphorylation	EDAVAAMSKDKANMQ HHHHHHHCCCCHHCC	32.73	-
349	2-Hydroxyisobutyrylation	VAAMSKDKANMQHRY HHHHCCCCHHCCHHH	45.45	-
349	Ubiquitination	VAAMSKDKANMQHRY HHHHCCCCHHCCHHH	45.45	21890473
356	Phosphorylation	KANMQHRYVELFLNS CHHCCHHHHHHHHHC	8.99	27251275
363	Phosphorylation	YVELFLNSTAGASGG HHHHHHHCCCCCCCC	23.06	28152594
364	Phosphorylation	VELFLNSTAGASGGA HHHHHHCCCCCCCCC	28.21	27251275
368	Phosphorylation	LNSTAGASGGAYEHR HHCCCCCCCCCCHHE	36.52	28152594
372	Phosphorylation	AGASGGAYEHRYVEL CCCCCCCCHHEEEEE	18.62	28152594
376	Phosphorylation	GGAYEHRYVELFLNS CCCCHHEEEEEEEEC	10.53	23879269
424	Phosphorylation	SGGYGGGYGGQSSMS CCCCCCCCCCCCCCC	22.74	26074081
428	Phosphorylation	GGGYGGQSSMSGYDQ CCCCCCCCCCCHHHH	31.14	26074081
429	Phosphorylation	GGYGGQSSMSGYDQV CCCCCCCCCCHHHHH	14.74	26074081
431	Phosphorylation	YGGQSSMSGYDQVLQ CCCCCCCCHHHHHHH	35.83	26074081
441	Phosphorylation	DQVLQENSSDFQSNI HHHHHHCCCHHHHHC	30.45	26074081
442	Phosphorylation	QVLQENSSDFQSNIA HHHHHCCCHHHHHCC	54.77	26074081
446	Phosphorylation	ENSSDFQSNIA---- HCCCHHHHHCC----	30.14	26074081

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
104	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HNRH1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HNRH1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPYL1_HUMAN	CRMP1	physical	16169070
HNRPF_HUMAN	HNRNPF	physical	9858532
TCPD_HUMAN	CCT4	physical	17643375
DDX17_HUMAN	DDX17	physical	17643375
DDX5_HUMAN	DDX5	physical	17643375
IMA1_HUMAN	KPNA2	physical	17643375
ROA1_HUMAN	HNRNPA1	physical	17643375
ROA2_HUMAN	HNRNPA2B1	physical	17643375
HNRPD_HUMAN	HNRNPD	physical	17643375
HNRPK_HUMAN	HNRNPK	physical	17643375
HNRPQ_HUMAN	SYNCRIP	physical	17643375
TCPE_HUMAN	CCT5	physical	17643375
CNOT9_HUMAN	RQCD1	physical	17643375
HNRH2_HUMAN	HNRNPH2	physical	17643375
HNRPU_HUMAN	HNRNPU	physical	17643375
YTHD2_HUMAN	YTHDF2	physical	17643375
FUBP2_HUMAN	KHSRP	physical	17643375
HNRPM_HUMAN	HNRNPM	physical	17643375
CPNE1_HUMAN	CPNE1	physical	17643375
YKT6_HUMAN	YKT6	physical	17643375
CH60_HUMAN	HSPD1	physical	17643375
HNRPF_HUMAN	HNRNPF	physical	22939629
ROA1_HUMAN	HNRNPA1	physical	22939629
HNRPR_HUMAN	HNRNPR	physical	22939629
RBMX_HUMAN	RBMX	physical	22939629
ROA2_HUMAN	HNRNPA2B1	physical	22939629
HNRH2_HUMAN	HNRNPH2	physical	22939629
HNRL1_HUMAN	HNRNPUL1	physical	22939629
ROA3_HUMAN	HNRNPA3	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
RU17_HUMAN	SNRNP70	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
HNRPL_HUMAN	HNRNPL	physical	22939629
RALY_HUMAN	RALY	physical	22939629
ILF2_HUMAN	ILF2	physical	22939629
HNRH3_HUMAN	HNRNPH3	physical	22939629
RAB5C_HUMAN	RAB5C	physical	22939629
IKIP_HUMAN	IKBIP	physical	22939629
YES_HUMAN	YES1	physical	22939629
TPP1_HUMAN	TPP1	physical	22939629
RBM4_HUMAN	RBM4	physical	22939629
PGRC1_HUMAN	PGRMC1	physical	22939629
NUP58_HUMAN	NUPL1	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
UBP7_HUMAN	USP7	physical	22939629
LS14A_HUMAN	LSM14A	physical	22939629
RBM14_HUMAN	RBM14	physical	22939629
CAVN1_HUMAN	PTRF	physical	22939629
SF3B4_HUMAN	SF3B4	physical	22365833
SF01_HUMAN	SF1	physical	22365833
RALY_HUMAN	RALY	physical	22365833
DDX5_HUMAN	DDX5	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
PP2AA_HUMAN	PPP2CA	physical	22863883
BASP1_HUMAN	BASP1	physical	26344197
ROAA_HUMAN	HNRNPAB	physical	26344197
NAMPT_HUMAN	NAMPT	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
KS6A3_HUMAN	RPS6KA3	physical	26344197
SCOC_HUMAN	SCOC	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HNRH1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-310, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-63; SER-104 ANDSER-310, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-104 ANDTHR-107, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-310, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-104 AND THR-107,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-310, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, AND MASSSPECTROMETRY.	15144186 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246 AND TYR-306, ANDMASS SPECTROMETRY.	15592455 [Abstract]